High level secretion of recombinant staphylokinase into periplasm of Escherichia coli

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The staphylokinase (SAK) gene from Staphylococcus aureus NCTC10033 was inserted into an expression vector, pKK-ompA, having a tac promoter and an ompA signal sequence. Escherichia coli JM109 carrying the recombinant plasmid produced and secreted the recombinant SAK (rSAK) at 15ug/ml into periplasm and 5ug/ml to extracellular media, respectively. The rSAK was purified with 59% yield by simple procedures from the periplasm of E. coli. The aminoterminal sequence and human plasminogen activating activity of rSAK were coincided with the authentic SAK.
Publisher
Springer
Issue Date
1998
Language
English
Article Type
Article
Keywords

EXPRESSION; STREPTOKINASE; MECHANISM; CLONING; GENE

Citation

BIOTECHNOLOGY LETTERS, v.20, no.2, pp.113 - 116

ISSN
0141-5492
URI
http://hdl.handle.net/10203/73217
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